ID   MDHC_YEAST              Reviewed;         377 AA.
AC   P22133;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 85.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
GN   Name=MDH2; OrderedLocusNames=YOL126C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17.
RX   MEDLINE=91094852; PubMed=1986231;
RA   Minard K.I., McAlister-Henn L.;
RT   "Isolation, nucleotide sequence analysis, and disruption of the MDH2
RT   gene from Saccharomyces cerevisiae: evidence for three isozymes of
RT   yeast malate dehydrogenase.";
RL   Mol. Cell. Biol. 11:370-380(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97051588; PubMed=8896265;
RX   DOI=10.1002/(SICI)1097-0061(199609)12:10B<1013::AID-YEA980>3.3.CO;2-X;
RA   Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E.,
RA   Arino J.;
RT   "Sequence analysis of a 13.4 kbp fragment from the left arm of
RT   chromosome XV reveals a malate dehydrogenase gene, a putative Ser/Thr
RT   protein kinase, the ribosomal L25 gene and four new open reading
RT   frames.";
RL   Yeast 12:1013-1020(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313270; PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-35.
RX   MEDLINE=87185517; PubMed=3552052; DOI=10.1016/0167-4838(87)90044-6;
RA   Kopetzki E., Entian K.-D., Lottspeich F., Mecke D.;
RT   "Purification procedure and N-terminal amino acid sequence of yeast
RT   malate dehydrogenase isoenzymes.";
RL   Biochim. Biophys. Acta 912:398-403(1987).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: The isoenzyme MDH2 may function primarily in the
CC       glyoxylate cycle.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       Q12154:GET3; NbExp=1; IntAct=EBI-10589, EBI-2989;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By acetate as carbon source in the growth medium. Is
CC       inactivated by addition of glucose (catabolite inactivation).
CC   -!- MISCELLANEOUS: Yeast contains at least 3 malate dehydrogenase
CC       isoenzymes: a mitochondrial (MDH1), a cytoplasmic (MDH2) and a
CC       peroxisomal (MDH3).
CC   -!- MISCELLANEOUS: Present with 5260 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
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DR   EMBL; M62808; AAA34766.1; -; Genomic_DNA.
DR   EMBL; U41293; AAC49466.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z74868; CAA99145.1; ALT_INIT; Genomic_DNA.
DR   PIR; S63444; DEBYMC.
DR   RefSeq; NP_014515.2; -.
DR   HSSP; P00346; 1MLD.
DR   DIP; DIP:4211N; -.
DR   IntAct; P22133; -.
DR   PeptideAtlas; P22133; -.
DR   Ensembl; YOL126C; Saccharomyces cerevisiae.
DR   GeneID; 853994; -.
DR   GenomeReviews; Y13140_GR; YOL126C.
DR   KEGG; sce:YOL126C; -.
DR   NMPDR; fig|4932.3.peg.5601; -.
DR   CYGD; YOL126c; -.
DR   SGD; S000005486; MDH2.
DR   HOGENOM; P22133; -.
DR   LinkHub; P22133; -.
DR   NextBio; 975482; -.
DR   ArrayExpress; P22133; -.
DR   GermOnline; YOL126C; Saccharomyces cerevisiae.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001557; L-lactate/malate_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DHase_AS.
DR   InterPro; IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11540:SF1; MDH_euk_g_bac; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; NAD;
KW   Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    377       Malate dehydrogenase, cytoplasmic.
FT                                /FTId=PRO_0000113338.
FT   NP_BIND      20     26       NAD (By similarity).
FT   NP_BIND     144    146       NAD (By similarity).
FT   ACT_SITE    215    215       Proton acceptor (By similarity).
FT   BINDING      57     57       NAD (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
FT   BINDING     119    119       NAD (By similarity).
FT   BINDING     146    146       Substrate (By similarity).
FT   BINDING     185    185       Substrate (By similarity).
FT   BINDING     266    266       NAD (By similarity).
FT   MOD_RES       6      6       Phosphothreonine.
SQ   SEQUENCE   377 AA;  40731 MW;  CAF4784FA7DD6E27 CRC64;
     MPHSVTPSIE QDSLKIAILG AAGGIGQSLS LLLKAQLQYQ LKESNRSVTH IHLALYDVNQ
     EAINGVTADL SHIDTPISVS SHSPAGGIEN CLHNASIVVI PAGVPRKPGM TRDDLFNVNA
     GIISQLGDSI AECCDLSKVF VLVISNPVNS LVPVMVSNIL KNHPQSRNSG IERRIMGVTK
     LDIVRASTFL REINIESGLT PRVNSMPDVP VIGGHSGETI IPLFSQSNFL SRLNEDQLKY
     LIHRVQYGGD EVVKAKNGKG SATLSMAHAG YKCVVQFVSL LLGNIEQIHG TYYVPLKDAN
     NFPIAPGADQ LLPLVDGADY FAIPLTITTK GVSYVDYDIV NRMNDMERNQ MLPICVSQLK
     KNIDKGLEFV ASRSASS
//